02001nas a2200217   4500008004100000022001400041245008000055210006900135260011000204300001600314490000700330520117500337100001801512700002201530700002201552700002401574700002601598700002801624700001801652856011301670       2015                        eng d  a1463-907600aCharge-switchable gold nanoparticles for enhanced enzymatic thermostability0 aChargeswitchable gold nanoparticles for enhanced enzymatic therm  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcJUL  a21517-215240 v173 a<p>This study illustrates a facile strategy for efficient immobilization of enzymes on a metal nanoparticle surface. The strategy proposed here enables the enzymatic activity to be retained while increasing the enzyme thermostability. It is demonstrated that the use of a zwitterionic amino acid tyrosine as a reducing and capping agent to synthesise gold nanoparticles allows efficient immobilization of phytase enzyme through charge-switchable electrostatic interactions. The detailed kinetic and thermodynamic studies reveal that the proposed enzyme immobilization strategy improves the overall quality of phytase by reducing the activation energy required for substrate hydrolysis and broadening the temperature window in which immobilized enzyme is able to operate. The outcomes of this study indicate that the underlying zwitterionic nature of 20 natural amino acids along with significant variability in their isoelectric points and hydropathy indices as well the ability of some of the amino acids to reduce metal ions is likely to offer significant opportunities for tailoring nano-bio interfaces in a rational manner for a range of biological applications.</p>1 aShankar, Shiv1 aSoni, Sarvesh, K.1 aDaima, Hemant, K.1 aSelvakannan, P., R.1 aKhire, Jayant, Malhar1 aBhargava, Suresh, Kumar1 aBansal, Vipul  uhttps://library.ncl.res.in/content/charge-switchable-gold-nanoparticles-enhanced-enzymatic-thermostability-0